Literature DB >> 14614155

Allosteric proteins: lessons to be learned from the hemoglobin intermediates.

Michele Perrella1, Rosaria Russo.   

Abstract

Allosteric proteins, such as hemoglobin, are assemblies of functional units, which undergo quaternary structural transitions in response to concentration changes of a specific ligand. Functional properties of hemoglobin ligation intermediates indicate that the tertiary structural changes induced by the ligand do not promote an equilibrium of quaternary structures.

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Year:  2003        PMID: 14614155     DOI: 10.1152/nips.01451.2003

Source DB:  PubMed          Journal:  News Physiol Sci        ISSN: 0886-1714


  2 in total

1.  Symmetric allosteric mechanism of hexameric Escherichia coli arginine repressor exploits competition between L-arginine ligands and resident arginine residues.

Authors:  Rebecca Strawn; Milan Melichercik; Michael Green; Thomas Stockner; Jannette Carey; Rüdiger Ettrich
Journal:  PLoS Comput Biol       Date:  2010-06-03       Impact factor: 4.475

Review 2.  Carbon Dioxide and the Carbamate Post-Translational Modification.

Authors:  Lynsay I Blake; Martin J Cann
Journal:  Front Mol Biosci       Date:  2022-03-01
  2 in total

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